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Database: UniProt
Entry: A0A151SE33_CAJCA
LinkDB: A0A151SE33_CAJCA
Original site: A0A151SE33_CAJCA 
ID   A0A151SE33_CAJCA        Unreviewed;       968 AA.
AC   A0A151SE33;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=KK1_025033 {ECO:0000313|EMBL:KYP53033.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP53033.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP53033.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; KQ483417; KYP53033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151SE33; -.
DR   STRING; 3821.A0A151SE33; -.
DR   OMA; KHIRISH; -.
DR   Proteomes; UP000075243; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 2.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075243}.
FT   REGION          360..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        708
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   968 AA;  108329 MW;  876353F60FA56081 CRC64;
     MTDITDDIAE EISFQSFDDD CRLLGNLLND ILQREVGTNL VDKIERIRVL AQSGCNMRQA
     GIVNMAELLE KQLASELSEM TLEEAFTLGR AFSHYLTLMG IAETHHRVRK GGNVAQIAKS
     CDDIFNQLVQ GGVPPDELYD TVCKQEVEIV LTAHPTQINR RTLQFKHIRI AHLLDYNDRP
     DLSVEDREMV IEDLVREITS IWQTDELRRQ KPTPVDEARA GFNIVDQSLW KAVPHYLRRV
     SNALKKHTGK PLPLTCTPIK FGSWMGGDRD GNPNVTAKVT KDVSLLSRWM AIDLYIREVD
     SLRFELSMNQ CSDRLSRLAH EILEANHEKH RRENWNQSVN RSHALPTQLP ARAHLPSFAE
     KGESQHPRLD IPGPDYMQSN HNKDGGVSLS STTLKNVSPN IRLSVTNSAN SSASSTANSS
     STFNSGQKKL YAEPQTGKST FQKLLEPMLP QLPGIAPYRI VLGNVKDKLE KSRRRLELLL
     EDVACDYDPL DYFETSDQLL EPLLLCYESL QSCGSGVLAD GRLADLIRRV ATFGMVLMKL
     DLRQESGRHA ETLDAITRYL DMGTYSEWDE EKKLDFLTRE LKGKRPLVPV SIEVPSDVKE
     VLDTFRIAAE LGSDSLGAYV ISMASNASDV LAVELLQKDA RLAAIGELGK ACPGGTLRVV
     PLFETVKDLR GAGSVIRKLL SIDWYREHII KNHNGHQEVM VGYSDSGKDA GRFTAAWELY
     KAQEDVVAAC NDYGIKVTLF HGRGGSIGRG GGPTYLAIQS QPPGSVMGTL RSTEQGEMVE
     AKFGLPQIAV RQLEIYTTAV LLATLRPPLP PREENWRNVM EEISNISCQS YRSVVYENPE
     FLSYFHEATP EAELGFLNIG SRPTRRKASR GIGHLRAIPW LFAWTQTRFV LPAWLGVGAG
     LKGACEKGHT EELKAMYKEW PFFQSTIDLI EMVLEILKRL RRDDDNLKIR DALLITINGI
     AAGMKNTG
//
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